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References from Disulfide bonds stabilize the SARS-CoV-2 RBD and preserve binding to ACE2 following thermal denaturation. Local targets link to admitted publications; unresolved targets remain external evidence.
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External reference
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
10.1126/science.abb2507 · 2020 · External reference
Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein
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Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM
10.1126/sciadv.abe5575 · 2021 · External reference
Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion
10.1038/s41586-020-2772-0 · 2020 · External reference
The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex
10.1128/jvi.77.16.8801-8811.2003 · 2003 · External reference
A pneumonia outbreak associated with a new coronavirus of probable bat origin
10.1038/s41586-020-2012-7 · 2020 · External reference
SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor
10.1016/j.cell.2020.02.052 · 2020 · External reference
Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses
10.1038/s41564-020-0688-y · 2020 · External reference
Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion
10.1073/pnas.1708727114 · 2017 · External reference
Enhanced isolation of SARS-CoV-2 by TMPRSS2-expressing cells
10.1073/pnas.2002589117 · 2020 · External reference
TMPRSS2 expression dictates the entry route used by SARS-CoV-2 to infect host cells
10.15252/embj.2021107821 · 2021 · External reference
TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells
10.26508/lsa.202000786 · 2020 · External reference
Cathepsin L plays a key role in SARS-CoV-2 infection in humans and humanized mice and is a promising target for new drug development
10.1038/s41392-021-00558-8 · 2021 · External reference
Mechanisms of SARS-CoV-2 entry into cells
10.1038/s41580-021-00418-x · 2022 · External reference
Site-specific glycan analysis of the SARS-CoV-2 spike
10.1126/science.abb9983 · 2020 · External reference
Site specific N- and O-glycosylation mapping of the spike proteins of SARS-CoV-2 variants of concern
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Quantitative profiling of N-glycosylation of SARS-CoV-2 spike protein variants
10.1093/glycob/cwad007 · 2023 · External reference
Role for N-glycans and calnexin-calreticulin chaperones in SARS-CoV-2 Spike maturation and viral infectivity
10.1126/sciadv.abq8678 · 2022 · External reference
10.1101/2020.06.26.173765
10.1101/2020.06.26.173765 · 2020 · External reference
A glycan gate controls opening of the SARS-CoV-2 spike protein
10.1038/s41557-021-00758-3 · 2021 · External reference
SARS-CoV-2 spike opening dynamics and energetics reveal the individual roles of glycans and their collective impact
10.1038/s42003-022-04138-6 · 2022 · External reference
Beyond shielding: the roles of glycans in the SARS-CoV-2 spike protein
10.1021/acscentsci.0c01056 · 2020 · External reference
Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition
10.1038/s41598-020-71748-7 · 2020 · External reference
Computational epitope map of SARS-CoV-2 spike protein
10.1371/journal.pcbi.1008790 · 2021 · External reference
SARS-CoV-2 simulations go exascale to predict dramatic spike opening and cryptic pockets across the proteome
10.1038/s41557-021-00707-0 · 2021 · External reference
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
10.1038/s41586-020-2180-5 · 2020 · External reference
Mapping neutralizing and immunodominant sites on the SARS-CoV-2 spike receptor-binding domain by structure-guided high-resolution serology
10.1016/j.cell.2020.09.037 · 2020 · External reference
Antibodies elicited by mRNA-1273 vaccination bind more broadly to the receptor binding domain than do those from SARS-CoV-2 infection
10.1126/scitranslmed.abi9915 · 2021 · External reference
The antigenic anatomy of SARS-CoV-2 receptor binding domain
10.1016/j.cell.2021.02.032 · 2021 · External reference
Comprehensive mapping of mutations in the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human plasma antibodies
10.1016/j.chom.2021.02.003 · 2021 · External reference
The receptor binding domain of SARS-CoV-2 spike is the key target of neutralizing antibody in human polyclonal sera
10.1101/2020.08.21.261727 · 2020 · External reference
Rapid generation of neutralizing antibody responses in COVID-19 patients
10.1016/j.xcrm.2020.100040 · 2020 · External reference
Cell entry mechanisms of SARS-CoV-2
10.1073/pnas.2003138117 · 2020 · External reference
Controlling the SARS-CoV-2 spike glycoprotein conformation
10.1038/s41594-020-0479-4 · 2020 · External reference
Modulation of SARS-CoV-2 spike binding to ACE2 through conformational selection
10.1038/s41565-025-01908-1 · 2025 · External reference
Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation
10.1038/s41594-020-0483-8 · 2020 · External reference
A thermostable, closed SARS-CoV-2 spike protein trimer
10.1038/s41594-020-0478-5 · 2020 · External reference
Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
10.1038/nature12711 · 2013 · External reference
Isolation and characterization of a novel bat coronavirus closely related to the direct progenitor of severe acute respiratory syndrome coronavirus
10.1128/jvi.02582-15 · 2016 · External reference
Discovery of a rich gene pool of bat SARS-related coronaviruses provides new insights into the origin of SARS coronavirus
10.1371/journal.ppat.1006698 · 2017 · External reference
Identification of novel bat coronaviruses sheds light on the evolutionary origins of SARS-CoV-2 and related viruses
10.1016/j.cell.2021.06.008 · 2021 · External reference
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
10.1038/nature02145 · 2003 · External reference
An ACE2-dependent Sarbecovirus in Russian bats is resistant to SARS-CoV-2 vaccines
10.1371/journal.ppat.1010828 · 2022 · External reference
Sarbecovirus RBD indels and specific residues dictating multi-species ACE2 adaptiveness
10.1038/s41467-024-53029-3 · 2024 · External reference
SARS-related coronavirus S-protein structures reveal synergistic RBM interactions underpinning high-affinity human ACE2 binding
10.1126/sciadv.adr8772 · 2025 · External reference
Cross-Species Virus Transmission and the Emergence of New Epidemic Diseases
10.1128/mmbr.00004-08 · 2008 · External reference
Molecular insights into receptor binding of recent emerging SARS-CoV-2 variants
10.1038/s41467-021-26401-w · 2021 · External reference
The alpha/B.1.1.7 SARS-CoV-2 variant exhibits significantly higher affinity for ACE-2 and requires lower inoculation doses to cause disease in K18-hACE2 mice
10.7554/elife.70002 · 2021 · External reference
Experimental evidence for enhanced receptor binding by rapidly spreading SARS-CoV-2 variants
10.1016/j.jmb.2021.167058 · 2021 · External reference
Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants
10.1126/science.abl8506 · 2021 · External reference
Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2
10.1016/j.cell.2022.01.001 · 2022 · External reference
Broader-species receptor binding and structural bases of Omicron SARS-CoV-2 to both mouse and palm-civet ACE2s
10.1038/s41421-022-00431-0 · 2022 · External reference
Structural basis of human ACE2 higher binding affinity to currently circulating Omicron SARS-CoV-2 sub-variants BA.2 and BA.1.1
10.1016/j.cell.2022.06.023 · 2022 · External reference
Neutralization of SARS-CoV-2 variants by convalescent and BNT162b2 vaccinated serum
10.1038/s41467-021-25479-6 · 2021 · External reference
SARS-CoV-2 variants B.1.351 and P.1 escape from neutralizing antibodies
10.1016/j.cell.2021.03.036 · 2021 · External reference
Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies
10.1038/s41591-021-01318-5 · 2021 · External reference
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7
10.1038/s41586-021-03398-2 · 2021 · External reference
Insights into SARS-CoV-2’s mutations for evading human antibodies: sacrifice and survival
10.1021/acs.jmedchem.1c00311 · 2022 · External reference
Cross-neutralization of SARS-CoV-2 B.1.1.7 and P.1 variants in vaccinated, convalescent and P.1 infected
10.1016/j.jinf.2021.07.019 · 2021 · External reference
SARS-CoV-2 spike E484K mutation reduces antibody neutralisation
10.1016/s2666-5247(21)00068-9 · 2021 · External reference
Reduced sensitivity of SARS-CoV-2 variant Delta to antibody neutralization
10.1038/s41586-021-03777-9 · 2021 · External reference
SARS-CoV-2 B.1.617.2 Delta variant replication and immune evasion
10.1038/s41586-021-03944-y · 2021 · External reference
Biophysical fitness landscape of the SARS-CoV-2 Delta variant receptor binding domain
10.1016/j.jmb.2022.167622 · 2022 · External reference
Antibody-mediated neutralization of authentic SARS-CoV-2 B.1.617 variants harboring L452R and T478K/E484Q
10.3390/v13091693 · 2021 · External reference
Delta variant (B.1.617.2) sublineages do not show increased neutralization resistance
10.1038/s41423-021-00772-y · 2021 · External reference
Considerable escape of SARS-CoV-2 Omicron to antibody neutralization
10.1038/s41586-021-04389-z · 2022 · External reference
Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2
10.1038/s41586-021-04388-0 · 2022 · External reference
Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
10.1038/s41586-021-04385-3 · 2022 · External reference
Neutralization of SARS-CoV-2 Omicron sub-lineages BA.1, BA.1.1, and BA.2
10.1016/j.chom.2022.04.014 · 2022 · External reference
SARS-CoV-2 BA.1 variant is neutralized by vaccine booster-elicited serum but evades most convalescent serum and therapeutic antibodies
10.1126/scitranslmed.abn8543 · 2022 · External reference
Omicron mutations enhance infectivity and reduce antibody neutralization of SARS-CoV-2 virus-like particles
10.1073/pnas.2200592119 · 2022 · External reference
SARS-CoV-2 Omicron is an immune escape variant with an altered cell entry pathway
10.1038/s41564-022-01143-7 · 2022 · External reference
Alarming antibody evasion properties of rising SARS-CoV-2 BQ and XBB subvariants
10.1016/j.cell.2022.12.018 · 2023 · External reference
Enhanced evasion of neutralizing antibody response by Omicron XBB.1.5, CH.1.1, and CA.3.1 variants
10.1016/j.celrep.2023.112443 · 2023 · External reference
Neutralising immunity to omicron sublineages BQ.1.1, XBB, and XBB.1.5 in healthy adults is boosted by bivalent BA.1-containing mRNA vaccination and previous Omicron infection
10.1016/s1473-3099(23)00289-x · 2023 · External reference
Humoral immune evasion of the omicron subvariants BQ.1.1 and XBB
10.1016/s1473-3099(22)00816-7 · 2023 · External reference
Virological characteristics of the SARS-CoV-2 Omicron BA.2 spike
10.1016/j.cell.2022.04.035 · 2022 · External reference
Expasy, the Swiss Bioinformatics Resource Portal, as designed by its users
10.1093/nar/gkab225 · 2021 · External reference
Disulfide bonds play a critical role in the structure and function of the receptor-binding domain of the SARS-CoV-2 spike antigen
10.1016/j.jmb.2021.167357 · 2022 · External reference
Impact of thiol-disulfide balance on the binding of Covid-19 spike protein with angiotensin-converting enzyme 2 receptor
10.1021/acsomega.0c02125 · 2020 · External reference
Disruption of disulfides within RBD of SARS-CoV-2 spike protein prevents fusion and represents a target for viral entry inhibition by registered drugs
10.1096/fj.202100560r · 2021 · External reference
The function of SARS-CoV-2 spike protein is impaired by disulfide-bond disruption with mutation at cysteine-488 and by thiol-reactive N-acetyl-cysteine and glutathione
10.1016/j.bbrc.2022.01.106 · 2022 · External reference
Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies
10.1016/s0168-1656(96)01636-7 · 1996 · External reference
The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation
10.1016/s0006-291x(03)00578-3 · 2003 · External reference
Role of arginine in the stabilization of proteins against aggregation
10.1021/bi047528r · 2005 · External reference
Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4
10.1038/cr.2013.92 · 2013 · External reference
Structure-based design of prefusion-stabilized SARS-CoV-2 spikes
10.1126/science.abd0826 · 2020 · External reference
Structural basis of receptor recognition by SARS-CoV-2
10.1038/s41586-020-2179-y · 2020 · External reference
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10.1073/pnas.1500851112 · 2015 · External reference
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10.1093/nar/gky497 · 2018 · External reference
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10.1093/bioinformatics/btm404 · 2007 · External reference
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